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Literature summary extracted from

  • Tanaka, N.; Nakanishi, M.; Kusakabe, Y.; Shiraiwa, K.; Yabe, S.; Ito, Y.; Kitade, Y.; Nakamura, K.T.
    Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum (2004), J. Mol. Biol., 343, 1007-1017.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.13.2.1 medicine SAHH inhibitors are expected to provide a new type of chemotherapeutic agent against malaria Plasmodium falciparum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.13.2.1 crystal structure of PfSAHH complexed with the reaction product adenosine. Crystals belong to an orthorhombic space group P2(1)2(1)2(1) with cell dimensions of a = 77.09 A, b = 86.15 A, and c = 333.8 A Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.13.2.1 additional information Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Plasmodium falciparum P50250
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 DL-homocysteine + adenosine
-
 Plasmodium falciparum S-adenosyl-DL-homocysteine + H2O
-
 ?
3.13.2.1 additional information S-adenosyl-L-homocysteine hydrolase is a regulator of biological methylations. Inhibitors of SAHH affect the methylation status of nucleic acids, proteins, and small molecules Plasmodium falciparum ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.13.2.1 SAHH
-
 Plasmodium falciparum